dbPTM

MOB1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MOB1A_HUMAN
UniProt AC	Q9H8S9
Protein Name	MOB kinase activator 1A
Gene Name	MOB1A
Organism	Homo sapiens (Human).
Sequence Length	216
Subcellular Localization
Protein Description	Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38..
Protein Sequence	MSFLFSSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFLFSSRS ------CCCCCCCCC	30.56	23401153
2	Acetylation	------MSFLFSSRS ------CCCCCCCCC	30.56	22814378
6	Phosphorylation	--MSFLFSSRSSKTF --CCCCCCCCCCCCC	27.30	28450419
7	Phosphorylation	-MSFLFSSRSSKTFK -CCCCCCCCCCCCCC	28.93	28450419
9	Phosphorylation	SFLFSSRSSKTFKPK CCCCCCCCCCCCCCC	37.83	28450419
10	Phosphorylation	FLFSSRSSKTFKPKK CCCCCCCCCCCCCCC	34.31	25159151
10	Ubiquitination	FLFSSRSSKTFKPKK CCCCCCCCCCCCCCC	34.31	23000965
11	Acetylation	LFSSRSSKTFKPKKN CCCCCCCCCCCCCCC	60.26	19823071
11	Ubiquitination	LFSSRSSKTFKPKKN CCCCCCCCCCCCCCC	60.26	23000965
12	Phosphorylation	FSSRSSKTFKPKKNI CCCCCCCCCCCCCCC	38.55	33259812
13	Ubiquitination	SSRSSKTFKPKKNIP CCCCCCCCCCCCCCC	17.11	23000965
14	Ubiquitination	SRSSKTFKPKKNIPE CCCCCCCCCCCCCCC	62.25	23000965
15	Ubiquitination	RSSKTFKPKKNIPEG CCCCCCCCCCCCCCC	48.97	23000965
16	Acetylation	SSKTFKPKKNIPEGS CCCCCCCCCCCCCCC	60.07	19823081
16	Ubiquitination	SSKTFKPKKNIPEGS CCCCCCCCCCCCCCC	60.07	23000965
17	Acetylation	SKTFKPKKNIPEGSH CCCCCCCCCCCCCCH	69.50	19823091
17	Ubiquitination	SKTFKPKKNIPEGSH CCCCCCCCCCCCCCH	69.50	23000965
23	Phosphorylation	KKNIPEGSHQYELLK CCCCCCCCHHHHHHH	13.02	17287340
26	Phosphorylation	IPEGSHQYELLKHAE CCCCCHHHHHHHHHH	11.79	28796482
29	Ubiquitination	GSHQYELLKHAEATL CCHHHHHHHHHHHHC	2.26	23000965
30	Ubiquitination	SHQYELLKHAEATLG CHHHHHHHHHHHHCC	54.09	23000965
35	Phosphorylation	LLKHAEATLGSGNLR HHHHHHHHCCCCCCE	24.13	29255136
38	Phosphorylation	HAEATLGSGNLRQAV HHHHHCCCCCCEEEE	27.85	25159151
53	Ubiquitination	MLPEGEDLNEWIAVN ECCCCCCHHHCCHHC	5.64	23000965
56	Ubiquitination	EGEDLNEWIAVNTVD CCCCHHHCCHHCHHH	5.24	23000965
58	Ubiquitination	EDLNEWIAVNTVDFF CCHHHCCHHCHHHHH	6.92	23000965
59	Ubiquitination	DLNEWIAVNTVDFFN CHHHCCHHCHHHHHH	4.55	23000965
72	Ubiquitination	FNQINMLYGTITEFC HHHHHHHHHHHHHHH	11.06	23000965
74	Phosphorylation	QINMLYGTITEFCTE HHHHHHHHHHHHHHH	15.92	18362890
95	Phosphorylation	SAGPRYEYHWADGTN CCCCCEEEECCCCCC	8.17	-
103	Ubiquitination	HWADGTNIKKPIKCS ECCCCCCCCCCCCCC	6.44	21890473
104 (in isoform 2)	Ubiquitination	-	55.34	21890473
104 (in isoform 1)	Ubiquitination	-	55.34	21890473
104	Ubiquitination	WADGTNIKKPIKCSA CCCCCCCCCCCCCCC	55.34	21890473
105	Ubiquitination	ADGTNIKKPIKCSAP CCCCCCCCCCCCCCC	48.45	23000965
107	Ubiquitination	GTNIKKPIKCSAPKY CCCCCCCCCCCCCHH	10.90	23000965
108	Ubiquitination	TNIKKPIKCSAPKYI CCCCCCCCCCCCHHH	30.57	23000965
141	Ubiquitination	SKIGVPFPKNFMSVA HHCCCCCCHHHHHHH	25.30	21890473
142 (in isoform 1)	Ubiquitination	-	64.30	21890473
142	Ubiquitination	KIGVPFPKNFMSVAK HCCCCCCHHHHHHHH	64.30	23000965
146	Ubiquitination	PFPKNFMSVAKTILK CCCHHHHHHHHHHHH	18.13	21890473
147	Ubiquitination	FPKNFMSVAKTILKR CCHHHHHHHHHHHHH	4.21	23000965
148	Acetylation	PKNFMSVAKTILKRL CHHHHHHHHHHHHHH	8.93	19608861
149	Acetylation	KNFMSVAKTILKRLF HHHHHHHHHHHHHHH	33.66	19608861
150	Ubiquitination	NFMSVAKTILKRLFR HHHHHHHHHHHHHHH	23.08	23000965
181	Phosphorylation	QEEAHLNTSFKHFIF HHHHHHCCCHHHHHH	41.73	14702039
184	Ubiquitination	AHLNTSFKHFIFFVQ HHHCCCHHHHHHHHH	37.06	21890473
191	Acetylation	KHFIFFVQEFNLIDR HHHHHHHHHCCCCCH	44.39	19608861
213	Ubiquitination	ELIEKLGSKDR---- HHHHHHCCCCC----	41.65	24816145
213	Phosphorylation	ELIEKLGSKDR---- HHHHHHCCCCC----	41.65	-
214	Ubiquitination	LIEKLGSKDR----- HHHHHCCCCC-----	56.58	24816145
256	Ubiquitination	----------------------------------------------- -----------------------------------------------		24816145

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
12	T	Phosphorylation	Kinase	STK3	Q13188	GPS
35	T	Phosphorylation	Kinase	STK3	Q13188	GPS
74	T	Phosphorylation	Kinase	STK3	Q13188	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MOB1A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MOB1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KXDL1_HUMAN	KXD1	physical	16189514
S10A8_HUMAN	S100A8	physical	17353931
NRDC_HUMAN	NRD1	physical	16061636
LATS1_HUMAN	LATS1	physical	16061636
LATS1_HUMAN	LATS1	physical	19739119
LATS2_HUMAN	LATS2	physical	19739119
A4_HUMAN	APP	physical	21832049
STK38_HUMAN	STK38	physical	15197186
AMOT_HUMAN	AMOT	physical	24255178
ANR28_HUMAN	ANKRD28	physical	24255178
ANR44_HUMAN	ANKRD44	physical	24255178
ANR52_HUMAN	ANKRD52	physical	24255178
CRLF3_HUMAN	CRLF3	physical	24255178
DOCK6_HUMAN	DOCK6	physical	24255178
DOCK7_HUMAN	DOCK7	physical	24255178
DOCK8_HUMAN	DOCK8	physical	24255178
DYST_HUMAN	DST	physical	24255178
IPO11_HUMAN	IPO11	physical	24255178
LATS1_HUMAN	LATS1	physical	24255178
LATS2_HUMAN	LATS2	physical	24255178
LRCH1_HUMAN	LRCH1	physical	24255178
LRCH2_HUMAN	LRCH2	physical	24255178
LRCH3_HUMAN	LRCH3	physical	24255178
MOB2_HUMAN	MOB2	physical	24255178
PPP6_HUMAN	PPP6C	physical	24255178
PP6R1_HUMAN	PPP6R1	physical	24255178
PP6R2_HUMAN	PPP6R2	physical	24255178
PP6R3_HUMAN	PPP6R3	physical	24255178
PTN14_HUMAN	PTPN14	physical	24255178
RASF2_HUMAN	RASSF2	physical	24255178
RASF5_HUMAN	RASSF5	physical	24255178
SAV1_HUMAN	SAV1	physical	24255178
STK3_HUMAN	STK3	physical	24255178
ST38L_HUMAN	STK38L	physical	24255178
STK4_HUMAN	STK4	physical	24255178
THOC2_HUMAN	THOC2	physical	24255178
1433F_HUMAN	YWHAH	physical	24255178
SEPT3_HUMAN	SEPT3	physical	25416956
CKLF3_HUMAN	CMTM3	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
LATS2_HUMAN	LATS2	physical	23886938

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MOB1A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT SER-2.	12665801 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2to form the scaffold to activate nuclear Dbf2-related kinase 1."; Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M.,Kawata A., Ohno K., Hata Y.; Oncogene 27:4281-4292(2008). Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, AND INTERACTION WITHSTK38 AND STK3/MST2.	18362890 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASSSPECTROMETRY.	18691976 [Abstract]